ID A0A553KAV2_9BACI Unreviewed; 139 AA. AC A0A553KAV2; DT 16-OCT-2019, integrated into UniProtKB/TrEMBL. DT 16-OCT-2019, sequence version 1. DT 27-MAR-2024, entry version 17. DE RecName: Full=biotin synthase {ECO:0000256|ARBA:ARBA00012236}; DE EC=2.8.1.6 {ECO:0000256|ARBA:ARBA00012236}; DE Flags: Fragment; GN ORFNames=FOI67_18180 {ECO:0000313|EMBL:TRY21761.1}; OS Geobacillus sp. LEMMJ02. OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=2595057 {ECO:0000313|EMBL:TRY21761.1, ECO:0000313|Proteomes:UP000319518}; RN [1] {ECO:0000313|EMBL:TRY21761.1, ECO:0000313|Proteomes:UP000319518} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LEMMJ02 {ECO:0000313|EMBL:TRY21761.1, RC ECO:0000313|Proteomes:UP000319518}; RA Schultz J., Kallies R., Da Rocha U.N., Rosado A.S.; RT "Genomes of thermophilic bacteria from Antarctica."; RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=(4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe- CC 2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + CC [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-2S]- CC [ferredoxin]; Xref=Rhea:RHEA:22060, Rhea:RHEA-COMP:10000, Rhea:RHEA- CC COMP:10001, Rhea:RHEA-COMP:14737, Rhea:RHEA-COMP:14739, CC ChEBI:CHEBI:17319, ChEBI:CHEBI:29917, ChEBI:CHEBI:33737, CC ChEBI:CHEBI:33738, ChEBI:CHEBI:57586, ChEBI:CHEBI:57844, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:64428, ChEBI:CHEBI:149473; EC=2.8.1.6; CC Evidence={ECO:0000256|ARBA:ARBA00023417}; CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8- CC diaminononanoate: step 2/2. {ECO:0000256|ARBA:ARBA00004942}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:TRY21761.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; VKJO01000264; TRY21761.1; -; Genomic_DNA. DR AlphaFoldDB; A0A553KAV2; -. DR UniPathway; UPA00078; UER00162. DR Proteomes; UP000319518; Unassembled WGS sequence. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0004076; F:biotin synthase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR002684; Biotin_synth/BioAB. DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM. DR InterPro; IPR007197; rSAM. DR PANTHER; PTHR22976; BIOTIN SYNTHASE; 1. DR PANTHER; PTHR22976:SF2; BIOTIN SYNTHASE, MITOCHONDRIAL; 1. DR Pfam; PF04055; Radical_SAM; 1. DR SMART; SM00729; Elp3; 1. DR SUPFAM; SSF102114; Radical SAM enzymes; 1. DR PROSITE; PS51918; RADICAL_SAM; 1. PE 4: Predicted; KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714}; KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485}; KW Biotin biosynthesis {ECO:0000256|ARBA:ARBA00022756}; KW Iron {ECO:0000256|ARBA:ARBA00023004}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}. FT DOMAIN 1..139 FT /note="Radical SAM core" FT /evidence="ECO:0000259|PROSITE:PS51918" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:TRY21761.1" FT NON_TER 139 FT /evidence="ECO:0000313|EMBL:TRY21761.1" SQ SEQUENCE 139 AA; 15120 MW; 031FAAC5E717511B CRC64; VASGRGPSDK EIDIVVSAVK EIKETYGLKV CACLGILKPE QALRLKEAGV DRYNHNINTS KEHHPHITTS HTYDDRVRTV ETVKEAGMSP CSGVIIGMKE TKQDVIAMAR SLKALDADSI PVNFLHAIDG TPLEGTKEL //